On the quaternary structure of a C-type lectin from Bothrops jararacussu venom--BJ-32 (BjcuL).
BJ-32 (also known as BjcuL) is a C-type lectin from the venom of Bothrops jararacussu with specificity for beta-galactosides and a remarkable ability to agglutinate several species of trypanosomatids. Our objective was to study the oligomerization state of native BJ-32 by using different biophysical and computational methods. Small-angle X-ray light scattering (SAXS) experiments disclosed a compact, globular protein with a radius of gyration of 36.72+/-0.04A and molecular weight calculated as 147.5+/-2.0kDa. From analytical ultracentrifugation analysis, it was determined that the BJ-32 sedimentation profile fits nicely to a decamer model. The analysis of the intrinsic emitted fluorescence spectra for BJ-32 solutions indicated that association of subunits in the decamer is accompanied by changes in the environment of Tryptophan residues. Both ab initio and comparative models of BJ-32 supported the resemblance of the decamer in the crystallographic structure from a close homologue, the rattlesnake venom lectin (RSL) from Crotalus atrox.
Silva
F P
FP
Laboratório de Bioquímica de Proteínas e Peptídeos, Instituto Oswaldo Cruz, Fiocruz, Av Brasil 4365, 21040-900 Rio de Janeiro, RJ, Brazil.
Alexandre
G M C
GM
Ramos
C H I
CH
De-Simone
S G
SG
D000595:Amino Acid Sequence; D000818:Animals; D017837:Bothrops; D002942:Circular Dichroism; D003198:Computer Simulation; D003435:Crotalid Venoms / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification; D037181:Lectins, C-Type / Q000032:analysis / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D053838:Scattering, Small Angle; D016415:Sequence Alignment; D021241:Spectrometry, Mass, Electrospray Ionization; D014461:Ultracentrifugation
C498078:BJcuL lectin, Bothrops jararacussu; D003435:Crotalid Venoms; D037181:Lectins, C-Type